Anti‐microbial peptides: from invertebrates to vertebrates

生物 抗菌肽 多细胞生物 测试表 先天免疫系统 肽序列 生物化学 蛋白质结构 基因 受体
作者
Philippe Bulet,Reto Stöcklin,Laure Menin
出处
期刊:Immunological Reviews [Wiley]
卷期号:198 (1): 169-184 被引量:1028
标识
DOI:10.1111/j.0105-2896.2004.0124.x
摘要

Summary: Gene‐encoded anti‐microbial peptides (AMPs) are widespread in nature, as they are synthesized by microorganisms as well as by multicellular organisms from both the vegetal and the animal kingdoms. These naturally occurring AMPs form a first line of host defense against pathogens and are involved in innate immunity. Depending on their tissue distribution, AMPs ensure either a systemic or a local protection of the organism against environmental pathogens. They are classified into three major groups: (i) peptides with an α‐helical conformation (insect cecropins, magainins, etc.), (ii) cyclic and open‐ended cyclic peptides with pairs of cysteine residues (defensins, protegrin, etc.), and (iii) peptides with an over‐representation of some amino acids (proline rich, histidine rich, etc.). Most AMPs display hydrophobic and cationic properties, have a molecular mass below 25–30 kDa, and adopt an amphipathic structure (α‐helix, β‐hairpin‐like β‐sheet, β‐sheet, or α‐helix/β‐sheet mixed structures) that is believed to be essential to their anti‐microbial action. Interestingly, in recent years, a series of novel AMPs have been discovered as processed forms of large proteins. Despite the extreme diversity in their primary and secondary structures, all natural AMPs have the in vitro particularity to affect a large number of microorganisms (bacteria, fungi, yeast, virus, etc.) with identical or complementary activity spectra. This review focuses on AMPs forming α‐helices, β‐hairpin‐like β‐sheets, β‐sheets, or α‐helix/β‐sheet mixed structures from invertebrate and vertebrate origins. These molecules show some promise for therapeutic use.

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